A method was developed for solubilization from bovine brain stem mitochondrial fraction of monoamine oxidases deminating biogenic amines. Preparative separation of the monoamine oxidases, possessing different substrate specificities, was achieved by column chromatography on a biospecific adsorbent AH-Sepharose 4 B. The enzyme preparations thus obtained did not contain any detectable by disc-electrophoresis of isoelectrofocusing in polyacrylamide gels proteins which were devoid of the monoamine oxidase activity.
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